Biotinidase

  • CAS Number: 9025-15-4

Biotinidase is an enzyme from the class of hydrolases, which releases the vitamin biotin from proteins. This is important for the taking place in the body recycling of biotin, but also in its absorption from the diet.

After investigation of the presence and distribution of biotinidase in the various organisms in the 1950s and 1960s, the enzyme moved from 1983 back to the scientific interest by the discovery that a biotinidase deficiency is the cause of a rare, inherited metabolic disease. The study of the various manifestations of the now designated as biotinidase defect (English biotinidase deficiency ) brought a number of new information on the function of biotinidase and the role of biotin in the body.

Occurrence

So far biotinidase was found except in people in various vertebrates as well as in fruit flies and fungi. Although differ Biotinidasen of various types, certain sections of the enzyme have been preserved during evolution. The family tree of biotinidase dates back to the Precambrian.

Also Some bacteria such as the lactic acid bacteria Lactobacillus casei or Enterococcus faecalis (formerly Streptococcus faecalis ) does not contain an enzyme that can liberate biotin, another lactic acid bacterium Lactobacillus arabinosus.

Structure

For some different creatures Biotinidasen from the complete sequence of amino acids in the protein is known. How has human biotinidase 523 amino acids of rat 521, in the mouse, there are 520 and 504 amino acids in the pufferfish. In other animals, only fragments could be sequenced.

Little is known about the three-dimensional structure. A crystal structure analysis so far failed due to the difficulty to crystallize biotinidase (as of early 2009 ). There is only a work based on computer simulation model, which according to the authors in detail, however, is uncertain.

Function

The biotinidase cleaves catalytically the resulting in the degradation of carboxylases biocytin into biotin and the amino acid lysine.

There is also evidence that the Biotinidase also plays a role as a transferase. According to experiments, in vitro, the enzyme is able to chemically bind biotin breakaway. Are histones present, possess the binding sites for biotin, they are biotinylated. The biotinidase is not the only enzyme that is capable of binding biotin to histones, which holocarboxylase synthetase also has this ability. However biotinidase is debiotinylieren also able histones. Which of the reactions take place at which histones under what conditions is the subject of current research. Epigenetic effects are discussed.

Genetics

The gene encoding the biotinidase is located in humans on chromosome 3 in the region p25. There are a number of known mutations that lead to a metabolic disease called multiple carboxylase deficiency. Meanwhile tested in many countries as part of newborn screening for biotinidase deficiency.

Documents

  • Hydrolase
  • Hereditary disease - associated protein
Human Genome Organisation CAS registry number Hydrolysis Opisthokont Drosophila melanogaster Tetraodontidae Protein crystallization Epigenetics
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